Ca2+-dependent Translocation of the Calcyclin-binding Protein in Neurons and Neuroblastoma NB-2a Cells

Filipek, Anna; Jastrzębska, Beata; Nowotny, Marcin; Kwiatkowska, Katarzyna; Hetman, Michał; Surmacz, Liliana; Wyroba, Elżbieta; Kuźnicki, Jacek

doi:10.1074/jbc.m111010200

Cited by 54 publications

(40 citation statements)

References 36 publications

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“…Results from others (Filipek et al, 2002b;Wu et al, 2003) and our studies suggest that phosphorylation and nuclear translocation are crucial for the function of SIP. We further demonstrate that phosphorylation at the Ser141 residue, the N-terminal region (aa 1-43) and the putative NLS region (aa 143-159) are crucial for nuclear translocation of SIP.…”

Section: Discussionsupporting

confidence: 69%

“…It has been revealed that SIP is phosphorylated by PKC in vitro (Filipek et al, 2002b) and curcumin activates PKC in a membrane-dependent and calciumregulated manner (Mahmmoud, 2007). In our study, both curcumin and PKC activator (PMA) cause SIP phosphorylation in MOLT-4 but not MOLT-4/AraG cells.…”

Section: Discussionmentioning

confidence: 46%

“…These data suggest that other modifications, besides the total amount of SIP protein, also contribute to the intensity change of SIP spot on 2D gel. It has been demonstrated that SIP is phosphorylated in unknown serine residues in neuroblastoma cells upon KCl or retinoic acid treatment (Filipek et al, 2002b;Wu et al, 2003). Furthermore, phosphorylation may cause changes in both isoelectric point and molecular weight of protein and therefore lead to the relocation of protein spots on 2D gel.…”

Section: Resultsmentioning

confidence: 99%

“…To verify whether the observed intensity change in SIP spot was due to the altered phosphorylation pattern of SIP, the whole cell extracts from MOLT-4 or MOLT-4/AraG treated with curcumin or DMSO were immunoprecipitated with anti-SIP, followed by immunoblotting with anti-phosphoserine antibody (Figure 2c). Cells treated with PMA, a protein kinase C (PKC) activator proved to induce SIP phosphorylation (Filipek et al, 2002b), served as a positive control. Interestingly, similar to PMA-treated cells, a strong band indicating phosphorylation in the serine residues of SIP was detected in curcumin-exposed MOLT-4 cells (Figure 2c, bottom left panel).…”

Section: Resultsmentioning

confidence: 99%

“…We next examined whether the cellular localization of SIP changed upon curcumin treatment, considering that it underwent both nuclear translocation and phosphorylation in KCl-or retinoic acid-treated cells (Filipek et al, 2002b;Wu et al, 2003). Using immunofluorescence staining, we found that curcumin exposure caused a significant translocation of endogenous SIP from the cytoplasm to nucleus in both MOLT-4 and MOLT-4/TG but not in MOLT-4/AraG cells ( Figure 3a).…”

Section: Resultsmentioning

confidence: 99%

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Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Luo

Yang

et al. 2010

Oncogene

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The mechanism underlying curcumin (diferuloylmethane) resistance is still largely unknown. Here we employed proteomic approach to identify the Siah-interacting protein (SIP) as a candidate for detailed study, because the spot intensity of SIP on a two-dimensional gel displayed 70-90% reduction in curcumin-sensitive cells, but remained unchanged in curcumin-resistant sublines, after curcumin treatment. Both gain-and loss-of-function studies revealed that SIP promoted curcumin-induced apoptosis. Moreover, SIP underwent phosphorylation and nuclear translocation in curcumin-sensitive but not resistant cells, upon curcumin exposure. The nuclear translocation of SIP was remarkably impaired when a putative nuclear localization sequence (NLS, amino acid (aa) 143-159) was deleted or the serine 141 was mutated into alanine, whereas truncation of the N-terminal region (aa 1-43) obviously increased the nuclear import of SIP. In accordance with their nuclear localization, N-terminal truncation significantly enhanced the proapoptotic effect of SIP, whereas NLS deletion or Ser141Ala mutation attenuated the apoptosis-promoting activity of both wildtype-and N-terminal truncated-SIP. These data suggest that SIP plays a role in apoptosis and curcumin resistance, and the function of SIP may be regulated by different motifs, such as the NLS, N-terminal region and serine 141. Our findings provide new insights into the biological significance of SIP and the mechanisms of drug resistance.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 46%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Luo

Yang

et al. 2010

Oncogene

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CacyBP/SIP inhibits Doxourbicin‐induced apoptosis of glioma cells due to activation of ERK1/2

et al. 2016

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Calcyclin-binding protein or Siah-1-interacting protein (CacyBP/SIP) was previously reported to promote the proliferation of glioma cells. However, the effect of CacyBP/SIP on apoptosis of glioma is poorly understood. Here, our study shows that CacyBP/SIP plays a role in inhibiting doxorubicin (DOX) induced apoptosis of glioma cells U251 and U87. Overexpression of CacyBP/SIP obviously suppressed the DOX-induced cell apoptosis. On the contrary, silencing of CacyBP/SIP significantly promoted it. Further investigation indicated that inhibition of apoptosis by CacyBP/SIP was relevant to its nuclear translocation in response to the DOX treatment. Importantly, we found that the level of p-ERK1/2 in nuclei was related to the nuclear accumulation of CacyBP/SIP. Finally, the role of CacyBP/SIP was confirmed in vivo in a mouse model with the cell line stably silencing CacyBP/SIP. Taken together, our results suggest that CacyBP/SIP plays an important role in inhibiting apoptosis of glioma cells which might be mediated by ERK1/2 signaling pathway, which will provide some guidance for the treatment of glioma. V C 2016 IUBMB Life, 68(3): [211][212][213][214][215][216][217][218][219] 2016

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Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

Xuan¹,

Gao²,

Jin³

et al. 2019

IUBMB Life

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The ubiquitin‐proteasome system is the primary cellular pathway for protein degradation, mediating 80% of intracellular protein degradation. Because of the widespread presence of ubiquitin‐modified protein substrates, ubiquitination can regulate a variety of cellular activities including cell proliferation, apoptosis, autophagy, endocytosis, DNA damage repair, and immune responses. With the continuous generation of genomics data in recent years it has become particularly important to analyze these data effectively and reasonably. Cacybp forms a complex with the E3 ubiquitinated ligase Siah1 to participate in ubiquitination. We analyzed Cacybp‐associated genes using the Gene Expression Omnibus (GEO) and CGGA (Chinese Glioma Genome Atlas) databases and identified 121 differentially expressed genes (DEGs), of which 46 were downregulated and 75 were upregulated. The biological processes, molecular functions, and protein–protein interaction (PPI) network of differential genes were analyzed by Cytoscape software and STRING software. We found no difference in Cacybp expression among different grades of gliomas and there was no significant association between the expression level of Cacybp and the prognosis of patients with glioma in LGG and GBM. © 2019 IUBMB Life, 1–8, 2019

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Ca2+-dependent Translocation of the Calcyclin-binding Protein in Neurons and Neuroblastoma NB-2a Cells

Cited by 54 publications

References 36 publications

Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

CacyBP/SIP inhibits Doxourbicin‐induced apoptosis of glioma cells due to activation of ERK1/2

Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

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